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Q8WWW0

- RASF5_HUMAN

UniProt

Q8WWW0 - RASF5_HUMAN

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Protein

Ras association domain-containing protein 5

Gene

RASSF5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Potential tumor suppressor. Seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. Isoform 2 stimulates lymphocyte polarization and the patch-like distribution of ITGAL/LFA-1, resulting in an enhanced adhesion to ICAM1. Together with RAP1A may participate in regulation of microtubule growth. The association of isoform 2 with activated RAP1A is required for directional movement of endothelial cells during wound healing. May be involved in regulation of Ras apoptotic function. The RASSF5-STK4/MST1 complex may mediate HRAS and KRAS induced apoptosis.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri122 – 17049Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. intracellular signal transduction Source: InterPro
  3. negative regulation of cell proliferation Source: Ensembl
  4. positive regulation of protein ubiquitination Source: Ensembl
  5. regulation of protein localization to nucleus Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ8WWW0.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras association domain-containing protein 5
Alternative name(s):
New ras effector 1
Regulator for cell adhesion and polarization enriched in lymphoid tissues
Short name:
RAPL
Gene namesi
Name:RASSF5
Synonyms:NORE1, RAPL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:17609. RASSF5.

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeleton
Note: Isoform 2 is mainly located in the perinuclear region of unstimulated primary T-cells. Upon stimulation translocates to the leading edge and colocalizes with ITGAL/LFA-1 in the peripheral zone of the immunological synapse. Isoform 2 is localized to growing microtubules in vascular endothelial cells and is dissociated from microtubules by activated RAP1A.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. microtubule Source: UniProtKB-KW
  3. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA134958571.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Ras association domain-containing protein 5PRO_0000240401Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei352 – 3521Phosphothreonine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8WWW0.
PaxDbiQ8WWW0.
PRIDEiQ8WWW0.

PTM databases

PhosphoSiteiQ8WWW0.

Expressioni

Tissue specificityi

Widely expressed. Frequently down-regulated in lung tumor cell lines and primary lung tumors.2 Publications

Gene expression databases

BgeeiQ8WWW0.
CleanExiHS_RASSF5.
ExpressionAtlasiQ8WWW0. differential.
GenevestigatoriQ8WWW0.

Organism-specific databases

HPAiCAB022664.

Interactioni

Subunit structurei

Interacts directly with activated HRAS; a RASSF5-STK4/MST1 complex probably associates with activated HRAS. Interacts with KRAS. Probably interacts with Ras-like GTPases RRAS, RRAS2, MRAS, RAP1B, RAP2A and RALA. Can self-associate. Interacts with RSSF1 isoform A. The RSSF1 isoform A-RSSF5 heterodimer probably mediates the association of RSSF1 with HRAS (By similarity). Isoform 2 interacts with activated RAP1A and ITGAL/LFA-1. Binds STK4/MST1, inhibiting STK4/MST1 autoactivation.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GABARAPO951662EBI-367390,EBI-712001
GABARAPL1Q9H0R82EBI-367390,EBI-746969
GABARAPL2P605202EBI-367390,EBI-720116
HRASP011122EBI-367390,EBI-350145
MAP1LC3BQ9GZQ85EBI-367390,EBI-373144
MAP1LC3CQ9BXW42EBI-367390,EBI-2603996
RAP1AP628343EBI-960502,EBI-491414
STK3Q131887EBI-367390,EBI-992580
STK4Q130437EBI-367390,EBI-367376

Protein-protein interaction databases

BioGridi123689. 29 interactions.
DIPiDIP-32490N.
IntActiQ8WWW0. 30 interactions.
STRINGi9606.ENSP00000347443.

Structurei

Secondary structure

1
418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi369 – 3713
Helixi374 – 41037

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LGDX-ray3.05E/F/G/H365-413[»]
4OH8X-ray2.28B366-418[»]
ProteinModelPortaliQ8WWW0.
SMRiQ8WWW0. Positions 113-170, 205-362, 366-413.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini274 – 36491Ras-associatingPROSITE-ProRule annotationAdd
BLAST
Domaini366 – 41348SARAHPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 Ras-associating domain.PROSITE-ProRule annotation
Contains 1 SARAH domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri122 – 17049Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG308852.
GeneTreeiENSGT00390000003367.
HOGENOMiHOG000013025.
HOVERGENiHBG054362.
InParanoidiQ8WWW0.
KOiK08015.
OMAiNCLLMKL.
OrthoDBiEOG7TF796.
PhylomeDBiQ8WWW0.
TreeFamiTF319243.

Family and domain databases

InterProiIPR002219. PE/DAG-bd.
IPR000159. Ras-assoc.
IPR011524. SARAH_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00788. RA. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
SM00314. RA. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50200. RA. 1 hit.
PS50951. SARAH. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8WWW0) [UniParc]FASTAAdd to Basket

Also known as: A, NORE1A

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAMASPAIGQ RPYPLLLDPE PPRYLQSLSG PELPPPPPDR SSRLCVPAPL
60 70 80 90 100
STAPGAREGR SARRAARGNL EPPPRASRPA RPLRPGLQQR LRRRPGAPRP
110 120 130 140 150
RDVRSIFEQP QDPRVPAERG EGHCFAELVL PGGPGWCDLC GREVLRQALR
160 170 180 190 200
CTNCKFTCHP ECRSLIQLDC SQQEGLSRDR PSPESTLTVT FSQNVCKPVE
210 220 230 240 250
ETQRPPTLQE IKQKIDSYNT REKNCLGMKL SEDGTYTGFI KVHLKLRRPV
260 270 280 290 300
TVPAGIRPQS IYDAIKEVNL AATTDKRTSF YLPLDAIKQL HISSTTTVSE
310 320 330 340 350
VIQGLLKKFM VVDNPQKFAL FKRIHKDGQV LFQKLSIADR PLYLRLLAGP
360 370 380 390 400
DTEVLSFVLK ENETGEVEWD AFSIPELQNF LTILEKEEQD KIQQVQKKYD
410
KFRQKLEEAL RESQGKPG
Length:418
Mass (Da):47,090
Last modified:March 1, 2002 - v1
Checksum:i4AFBC69B1325CC9E
GO
Isoform 2 (identifier: Q8WWW0-2) [UniParc]FASTAAdd to Basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     1-153: Missing.
     154-193: CKFTCHPECR...ESTLTVTFSQ → MTVDSSMSSG...RNAQSKHLSK

Note: Initiator Met-1 is removed. Contains a N-acetylthreonine at position 2.

Show »
Length:265
Mass (Da):30,359
Checksum:i66AD5D84EFA6D6CB
GO
Isoform 3 (identifier: Q8WWW0-3) [UniParc]FASTAAdd to Basket

Also known as: C, NORE1B

The sequence of this isoform differs from the canonical sequence as follows:
     331-336: LFQKLS → GCLLHP
     337-418: Missing.

Show »
Length:336
Mass (Da):37,433
Checksum:i2657B6DAECD8D6A9
GO

Sequence cautioni

The sequence AAH04270.1 differs from that shown. Reason: Aberrant splicing.
The sequence AAH07203.1 differs from that shown. Reason: Aberrant splicing.
The sequence AAH04270.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH07203.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 153153Missing in isoform 2. 5 PublicationsVSP_019363Add
BLAST
Alternative sequencei154 – 19340CKFTC…VTFSQ → MTVDSSMSSGYCSLDEELED CFFTAKTTFFRNAQSKHLSK in isoform 2. 5 PublicationsVSP_019364Add
BLAST
Alternative sequencei331 – 3366LFQKLS → GCLLHP in isoform 3. 1 PublicationVSP_019365
Alternative sequencei337 – 41882Missing in isoform 3. 1 PublicationVSP_019366Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF445801 mRNA. Translation: AAL38592.1.
AY261332 mRNA. Translation: AAP83360.1.
AY062002 mRNA. Translation: AAL40388.1.
AY062003 mRNA. Translation: AAL40389.1.
AY216268 mRNA. Translation: AAO61668.1.
AK289861 mRNA. Translation: BAF82550.1.
AL832784 mRNA. Translation: CAI46164.1.
AL591846, AL354681 Genomic DNA. Translation: CAI13536.1.
AL591846, AL354681 Genomic DNA. Translation: CAI13538.1.
AL354681, AL591846 Genomic DNA. Translation: CAI15252.1.
AL591846, AL354681 Genomic DNA. Translation: CAI13537.1.
AL591846, AL354681 Genomic DNA. Translation: CAI13542.1.
AL354681, AL591846 Genomic DNA. Translation: CAI15253.1.
AL354681, AL591846 Genomic DNA. Translation: CAI15254.1.
AL354681, AL591846 Genomic DNA. Translation: CAI15256.1.
CH471100 Genomic DNA. Translation: EAW93544.1.
BC004270 mRNA. Translation: AAH04270.1. Sequence problems.
BC007203 mRNA. Translation: AAH07203.1. Sequence problems.
BC042651 mRNA. Translation: AAH42651.1.
CCDSiCCDS1463.1. [Q8WWW0-3]
CCDS1464.1. [Q8WWW0-2]
CCDS30998.1. [Q8WWW0-1]
RefSeqiNP_872604.1. NM_182663.3. [Q8WWW0-1]
NP_872605.1. NM_182664.3. [Q8WWW0-3]
NP_872606.1. NM_182665.3. [Q8WWW0-2]
UniGeneiHs.497579.

Genome annotation databases

EnsembliENST00000577571; ENSP00000462576; ENSG00000266094. [Q8WWW0-2]
ENST00000579436; ENSP00000462099; ENSG00000266094. [Q8WWW0-1]
ENST00000580449; ENSP00000462544; ENSG00000266094. [Q8WWW0-3]
GeneIDi83593.
KEGGihsa:83593.
UCSCiuc001hed.3. human. [Q8WWW0-1]
uc001hee.3. human. [Q8WWW0-3]
uc001hef.3. human. [Q8WWW0-2]

Polymorphism databases

DMDMi74751587.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF445801 mRNA. Translation: AAL38592.1 .
AY261332 mRNA. Translation: AAP83360.1 .
AY062002 mRNA. Translation: AAL40388.1 .
AY062003 mRNA. Translation: AAL40389.1 .
AY216268 mRNA. Translation: AAO61668.1 .
AK289861 mRNA. Translation: BAF82550.1 .
AL832784 mRNA. Translation: CAI46164.1 .
AL591846 , AL354681 Genomic DNA. Translation: CAI13536.1 .
AL591846 , AL354681 Genomic DNA. Translation: CAI13538.1 .
AL354681 , AL591846 Genomic DNA. Translation: CAI15252.1 .
AL591846 , AL354681 Genomic DNA. Translation: CAI13537.1 .
AL591846 , AL354681 Genomic DNA. Translation: CAI13542.1 .
AL354681 , AL591846 Genomic DNA. Translation: CAI15253.1 .
AL354681 , AL591846 Genomic DNA. Translation: CAI15254.1 .
AL354681 , AL591846 Genomic DNA. Translation: CAI15256.1 .
CH471100 Genomic DNA. Translation: EAW93544.1 .
BC004270 mRNA. Translation: AAH04270.1 . Sequence problems.
BC007203 mRNA. Translation: AAH07203.1 . Sequence problems.
BC042651 mRNA. Translation: AAH42651.1 .
CCDSi CCDS1463.1. [Q8WWW0-3 ]
CCDS1464.1. [Q8WWW0-2 ]
CCDS30998.1. [Q8WWW0-1 ]
RefSeqi NP_872604.1. NM_182663.3. [Q8WWW0-1 ]
NP_872605.1. NM_182664.3. [Q8WWW0-3 ]
NP_872606.1. NM_182665.3. [Q8WWW0-2 ]
UniGenei Hs.497579.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4LGD X-ray 3.05 E/F/G/H 365-413 [» ]
4OH8 X-ray 2.28 B 366-418 [» ]
ProteinModelPortali Q8WWW0.
SMRi Q8WWW0. Positions 113-170, 205-362, 366-413.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123689. 29 interactions.
DIPi DIP-32490N.
IntActi Q8WWW0. 30 interactions.
STRINGi 9606.ENSP00000347443.

PTM databases

PhosphoSitei Q8WWW0.

Polymorphism databases

DMDMi 74751587.

Proteomic databases

MaxQBi Q8WWW0.
PaxDbi Q8WWW0.
PRIDEi Q8WWW0.

Protocols and materials databases

DNASUi 83593.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000577571 ; ENSP00000462576 ; ENSG00000266094 . [Q8WWW0-2 ]
ENST00000579436 ; ENSP00000462099 ; ENSG00000266094 . [Q8WWW0-1 ]
ENST00000580449 ; ENSP00000462544 ; ENSG00000266094 . [Q8WWW0-3 ]
GeneIDi 83593.
KEGGi hsa:83593.
UCSCi uc001hed.3. human. [Q8WWW0-1 ]
uc001hee.3. human. [Q8WWW0-3 ]
uc001hef.3. human. [Q8WWW0-2 ]

Organism-specific databases

CTDi 83593.
GeneCardsi GC01P206680.
HGNCi HGNC:17609. RASSF5.
HPAi CAB022664.
MIMi 607020. gene.
neXtProti NX_Q8WWW0.
PharmGKBi PA134958571.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG308852.
GeneTreei ENSGT00390000003367.
HOGENOMi HOG000013025.
HOVERGENi HBG054362.
InParanoidi Q8WWW0.
KOi K08015.
OMAi NCLLMKL.
OrthoDBi EOG7TF796.
PhylomeDBi Q8WWW0.
TreeFami TF319243.

Enzyme and pathway databases

SignaLinki Q8WWW0.

Miscellaneous databases

GeneWikii RASSF5.
GenomeRNAii 83593.
NextBioi 72517.
PROi Q8WWW0.
SOURCEi Search...

Gene expression databases

Bgeei Q8WWW0.
CleanExi HS_RASSF5.
ExpressionAtlasi Q8WWW0. differential.
Genevestigatori Q8WWW0.

Family and domain databases

InterProi IPR002219. PE/DAG-bd.
IPR000159. Ras-assoc.
IPR011524. SARAH_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF00130. C1_1. 1 hit.
PF00788. RA. 1 hit.
[Graphical view ]
SMARTi SM00109. C1. 1 hit.
SM00314. RA. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
PROSITEi PS50200. RA. 1 hit.
PS50951. SARAH. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "RASSF3 and NORE1: identification and cloning of two human homologues of the putative tumor suppressor gene RASSF1."
    Tommasi S., Dammann R., Jin S.-G., Zhang X.-F., Avruch J., Pfeifer G.P.
    Oncogene 21:2713-2720(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  2. "RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1."
    Katagiri K., Maeda A., Shimonaka M., Kinashi T.
    Nat. Immunol. 4:741-748(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN INTEGRIN ACTIVATION, INTERACTION WITH RAP1A AND ITGAL, SUBCELLULAR LOCATION.
  3. "RASSF3 is regulated by methylation in lung and breast tumor cell lines."
    Burbee D.G., White M.A., Minna J.D.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Lymph node.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Skin.
  9. "The pro-apoptotic Ras effector Nore1 may serve as a Ras-regulated tumor suppressor in the lung."
    Vos M.D., Martinez A., Ellis C.A., Vallecorsa T., Clark G.J.
    J. Biol. Chem. 278:21938-21943(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A TUMOR SUPPRESSOR, TISSUE SPECIFICITY.
  10. "Regulation of the MST1 kinase by autophosphorylation, by the growth inhibitory proteins, RASSF1 and NORE1, and by Ras."
    Praskova M., Khoklatchev A., Ortiz-Vega S., Avruch J.
    Biochem. J. 381:453-462(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STK4/MST1.
  11. "Local activation of Rap1 contributes to directional vascular endothelial cell migration accompanied by extension of microtubules on which RAPL, a Rap1-associating molecule, localizes."
    Fujita H., Fukuhara S., Sakurai A., Yamagishi A., Kamioka Y., Nakaoka Y., Masuda M., Mochizuki N.
    J. Biol. Chem. 280:5022-5031(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MICROTUBULE GROWTH REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH RAP1A.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRASF5_HUMAN
AccessioniPrimary (citable) accession number: Q8WWW0
Secondary accession number(s): A8K1E6
, Q5SY32, Q8WWV9, Q8WXF4, Q9BT99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 1, 2002
Last modified: October 29, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3